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Vol. 62, Issue 4, 806-816, October 2002
Department of Biology, University of South Florida, Tampa, Florida
Changes in the concentration or subcellular location of the key
proteins involved in signal transduction pathways have been shown to
impact gene regulation. Studies were designed to evaluate the
relationship between aryl hydrocarbon receptor (AHR) localization, stability, and gene regulation in a defined system where the endogenous AHR protein could be evaluated. The findings indicate that treatment of
cells with geldanamycin (GA) or MG-132 (an inhibitor of the 26S
proteasome) results in nuclear translocation of the endogenous AHR in
both human HepG2 and murine Hepa-1 cells without induction of
endogenous CYP1A1 protein. Exposure to GA resulted in the degradation of AHR by >90% in the nucleus via the 26S proteasome. Importantly, the reduced level of AHR resulted in a 50% reduction in the maximal level of CYP1A1 induced by
2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). In all
treatments the concentration of the AHR nuclear translocator (ARNT)
protein was unchanged and had no impact on the localization of the AHR.
Thus, ligand-independent translocation of the AHR to the nucleus was
not sufficient to induce CYP1A1 in the absence of ligand, but
reductions in the level of the endogenous AHR protein pool shifted the
dose-response curve for TCDD to the right.
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